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Literature summary extracted from

  • Matsumura, H.; Matsuda, K.; Nakamura, N.; Ohtaki, A.; Yoshida, H.; Kamitori, S.; Yohda, M.; Ohno, H.
    Monooxygenation by a thermophilic cytochrome P450 via direct electron donation from NADH (2011), Metallomics, 3, 389-395.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.B28 wild-type enzyme and F-G loop deletion mutant enzyme delLL151-E156, overexpression in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.B28 vapour diffusion method, X-ray crystallography at a resolution of 1.94 A reveals a sufficiently large heme pocket for NAD(P)H binding and a novel contiguous channel from the active site to bulk solvent in the distal heme pocket. The mutant shows a higher affinity for NADH compared with the wild-type because the mutant has a more widely open distal pocket for NAD(P)H binding Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.B28 delL151-E156 the Km value of the mutant is about 2times lower than that of the wild-type. Sulfurisphaera tokodaii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.B28 0.29
-
 Styrene pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
1.14.13.B28 0.52
-
 Styrene pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
1.14.13.B28 7
-
 NADH pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
1.14.13.B28 13
-
 NADH pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.B28 43000
-
 F-G loop deletion mutant enzyme delLL151-E156 Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.B28 Sulfurisphaera tokodaii Q972I2
-
-
1.14.13.B28 Sulfurisphaera tokodaii 7 Q972I2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.B28
-
 Sulfurisphaera tokodaii

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.B28 styrene + NADH + H+ + O2 = styrene epoxide + NAD+ + H2O sequential mechanism. Both styrene and NADH bind to the enzyme before any product is released Sulfurisphaera tokodaii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.B28 styrene + NADH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii styrene epoxide + NAD+ + H2O
-
 ?
1.14.13.B28 styrene + NADH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii 7 styrene epoxide + NAD+ + H2O
-
 ?
1.14.13.B28 styrene + NADPH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii styrene epoxide + NADP+ + H2O
-
 ?
1.14.13.B28 styrene + NADPH + H+ + O2 the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii 7 styrene epoxide + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.B28 P450st
-
 Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.B28 25
-
 assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.B28 0.000057
-
 Styrene pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii
1.14.13.B28 0.000061
-
 Styrene pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
1.14.13.B28 0.000076
-
 NADH pH 7, 25°C, wild-type enzyme Sulfurisphaera tokodaii
1.14.13.B28 0.000079
-
 NADH pH 7, 25°C, mutant enzyme delLL151-E156 Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.B28 7
-
 assay at Sulfurisphaera tokodaii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.B28 NADH the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii
1.14.13.B28 NADPH the initial rate of catalysis with NADH is slightly higher than with NADPH Sulfurisphaera tokodaii